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Protein

Metallo-beta-lactamase type 2

Gene

blaB4

Organism
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring.By similarity

Catalytic activityi

A beta-lactam + H2O = a substituted beta-amino acid.By similarity

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi98 – 981Zinc 1; via tele nitrogenBy similarity
Metal bindingi100 – 1001Zinc 1; via pros nitrogenBy similarity
Metal bindingi102 – 1021Zinc 2By similarity
Metal bindingi161 – 1611Zinc 1; via tele nitrogenBy similarity
Metal bindingi180 – 1801Zinc 2By similarity
Binding sitei183 – 1831SubstrateBy similarity
Metal bindingi222 – 2221Zinc 2; via tele nitrogenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Metallo-beta-lactamase type 2Curated (EC:3.5.2.6By similarity)
Alternative name(s):
B2 metallo-beta-lactamaseBy similarity
Beta-lactamase type IIBy similarity
Carbapenem-hydrolyzing beta-lactamase BlaB-4By similarity
Short name:
CHbetaL-4By similarity
Class B carbapenemase BlaB-4By similarity
Metallo lactamase BlaB-31 Publication
Metallo-beta-lactamase type IIBy similarity
Gene namesi
Name:blaB4
Synonyms:blaBBy similarity, blaB31 Publication
OrganismiElizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Taxonomic identifieri238 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisBy similarity1 PublicationAdd
BLAST
Chaini23 – 249227Metallo-beta-lactamase type 2PRO_0000016952Add
BLAST

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9XBN7.
SMRiQ9XBN7. Positions 27-245.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001018. Beta-lactamase_class-B_CS.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PfamiPF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
PROSITEiPS00743. BETA_LACTAMASE_B_1. 1 hit.
PS00744. BETA_LACTAMASE_B_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9XBN7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMKKMKWALV LALGLTGLNA FGQETPEVKI EKLKDNLYVY TTYNTFNGTK
60 70 80 90 100
YAANAVYLVT SKGVVVIDSP WGEEKFKNFT DEIYKRHGKK VIMNIATHSH
110 120 130 140 150
DDRAGGLEYF KSLGAKTYST KMTDSILAKD NKPRAQYTFD NNKSFKVGKD
160 170 180 190 200
EFQVYYPGKG HTADHVVVWF PKDKVLVGGC IIKSGDSKDL GFLGEAYVND
210 220 230 240
WTQSVHNIQK KFPNVQYVVA GHDDWKDQTA IQHTLDLISE YQQKQKASN
Length:249
Mass (Da):28,225
Last modified:November 1, 1999 - v1
Checksum:iF5327FD6516153B5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF162284 Genomic DNA. Translation: AAD43582.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF162284 Genomic DNA. Translation: AAD43582.1.

3D structure databases

ProteinModelPortaliQ9XBN7.
SMRiQ9XBN7. Positions 27-245.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001018. Beta-lactamase_class-B_CS.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PfamiPF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
PROSITEiPS00743. BETA_LACTAMASE_B_1. 1 hit.
PS00744. BETA_LACTAMASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Carbapenemases of chryseobacterium (Flavobacterium) meningosepticum: distribution of blaB and characterization of a novel metallo-beta-lactamase gene, blaB3, in the type strain, NCTC 10016."
    Woodford N., Palepou M.-F.I., Babini G.S., Holmes B., Livermore D.M.
    Antimicrob. Agents Chemother. 44:1448-1452(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 13253 / CIP 60.57 / DSM 2800 / LMG 12279 / NBRC 12535 / NCTC 10016.
  2. "Molecular and biochemical heterogeneity of class B carbapenem-hydrolyzing beta-lactamases in Chryseobacterium meningosepticum."
    Bellais S., Aubert D., Naas T., Nordmann P.
    Antimicrob. Agents Chemother. 44:1878-1886(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 13253 / CIP 60.57 / DSM 2800 / LMG 12279 / NBRC 12535 / NCTC 10016.

Entry informationi

Entry nameiBLAB4_ELIME
AccessioniPrimary (citable) accession number: Q9XBN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.